Purification and characterization of an oxidation-stable, thiol-dependent serine alkaline protease from Bacillus mojavensis

382 citations recorded by the source corpus.

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

Production dynamics of extracellular protease from Bacillus species (2005, background): “3.4.24) constitute one of the most important groups of industrial enzymes accounting for about 60% of the total worldwide enzyme sales (Nascimento and Martins, 2004; Beg and Gupta, 2003; Ellaiah et al., 2003).”
Deep-sea fungi as a source of alkaline and cold-tolerant proteases (2006, background): “6 unit is equivalent to μg tyrosine released mL min [20].”
Keratinolytic proteases of Bacillus species isolated from the Amazon basin showing remarkable de-hairing activity (2007, background): “In addition, the enzymes were active on a broad range of protein substrates, were not inhibited by detergents, and were active at alkaline pH suggesting they are useful for purposes such as laundry ( Beg and Gupta 2003 ).”
A novel surfactant-stable alkaline serine-protease from a newly isolated Bacillus mojavensis A21. Purification and characterization (2009, background): “The improvement in protease thermostability against thermal inactivation in the presence of CaCl2 may be explained by the strengthening of interactions inside protein molecules and probably by the binding of Ca to autolysis site [12,31].”